BTRK_NIACI
ID BTRK_NIACI Reviewed; 428 AA.
AC Q2L4H3; Q4H4E6;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=L-glutamyl-[BtrI acyl-carrier protein] decarboxylase;
DE EC=4.1.1.95;
DE AltName: Full=Butirosin biosynthesis protein K;
GN Name=btrK;
OS Niallia circulans (Bacillus circulans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Niallia.
OX NCBI_TaxID=1397;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RX PubMed=16156513; DOI=10.1038/ja.2005.47;
RA Kudo F., Numakura M., Tamegai H., Yamamoto H., Eguchi T., Kakinuma K.;
RT "Extended sequence and functional analysis of the butirosin biosynthetic
RT gene cluster in Bacillus circulans SANK 72073.";
RL J. Antibiot. 58:373-379(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RA Aboshanab K.M., Schmidt-Beissner H., Wehmeier U.F., Welzel K., Vente A.,
RA Piepersberg W.;
RT "Analysis and comparison of the biosynthetic gene clusters for the 2-
RT deoxystreptamine-containing aminoglycoside antibiotics ribostamycin,
RT neomycin, lividomycin, paromomycin and butirosin.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR, AND SUBUNIT.
RC STRAIN=ATCC 21557 / NCIMB 12336 / BU-1709-YQW-B6;
RX PubMed=15975512; DOI=10.1016/j.chembiol.2005.04.010;
RA Li Y., Llewellyn N.M., Giri R., Huang F., Spencer J.B.;
RT "Biosynthesis of the unique amino acid side chain of butirosin: possible
RT protective-group chemistry in an acyl carrier protein-mediated pathway.";
RL Chem. Biol. 12:665-675(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE,
RP AND COFACTOR.
RA Popovic B., Li Y., Chirgadze D.Y., Blundell T.L., Spencer J.B.;
RT "Structural characterisation of Btrk decarboxylase from Bacillus circulans
RT butirosin biosynthesis.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Pyridoxal phosphate-dependent decarboxylase that catalyzes 1
CC step in the biosynthesis of the side chain of the aminoglycoside
CC antibiotics in the biosynthetic pathway of butirosin. Able to
CC decarboxylate L-ornithine, L-arginine, L-lysine, but not L-glutamate or
CC any D-amino acids. Has low activity with substrates not bound to an
CC acyl-carrier protein. {ECO:0000269|PubMed:15975512}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=gamma-L-glutamyl-[BtrI ACP] + H(+) = 4-aminobutanoyl-[BtrI
CC ACP] + CO2; Xref=Rhea:RHEA:53956, Rhea:RHEA-COMP:13742, Rhea:RHEA-
CC COMP:13744, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:137996,
CC ChEBI:CHEBI:137997; EC=4.1.1.95;
CC Evidence={ECO:0000269|PubMed:15975512};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:15975512, ECO:0000269|Ref.4};
CC -!- PATHWAY: Antibiotic biosynthesis; butirosin biosynthesis.
CC {ECO:0000269|PubMed:15975512}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15975512, ECO:0000269|Ref.4}.
CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAG77429.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB097196; BAE07075.1; -; Genomic_DNA.
DR EMBL; AJ781030; CAG77429.1; ALT_INIT; Genomic_DNA.
DR PDB; 2J66; X-ray; 1.65 A; A=1-428.
DR PDBsum; 2J66; -.
DR AlphaFoldDB; Q2L4H3; -.
DR SMR; Q2L4H3; -.
DR PRIDE; Q2L4H3; -.
DR KEGG; ag:BAE07075; -.
DR BioCyc; MetaCyc:MON-17273; -.
DR UniPathway; UPA00964; -.
DR GO; GO:0016831; F:carboxy-lyase activity; IDA:UniProtKB.
DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IDA:UniProtKB.
DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro.
DR Gene3D; 2.40.37.10; -; 1.
DR Gene3D; 3.20.20.10; -; 1.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR002986; DAP_deCOOHase_LysA.
DR InterPro; IPR022643; De-COase2_C.
DR InterPro; IPR022657; De-COase2_CS.
DR InterPro; IPR022644; De-COase2_N.
DR InterPro; IPR000183; Orn/DAP/Arg_de-COase.
DR InterPro; IPR029066; PLP-binding_barrel.
DR Pfam; PF02784; Orn_Arg_deC_N; 1.
DR Pfam; PF00278; Orn_DAP_Arg_deC; 1.
DR PRINTS; PR01181; DAPDCRBXLASE.
DR PRINTS; PR01179; ODADCRBXLASE.
DR SUPFAM; SSF50621; SSF50621; 1.
DR SUPFAM; SSF51419; SSF51419; 1.
DR PROSITE; PS00879; ODR_DC_2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Decarboxylase; Lyase;
KW Pyridoxal phosphate.
FT CHAIN 1..428
FT /note="L-glutamyl-[BtrI acyl-carrier protein]
FT decarboxylase"
FT /id="PRO_0000421756"
FT BINDING 228
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 269..272
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250"
FT BINDING 375
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 49
FT /note="N6-(pyridoxal phosphate)lysine"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 24..36
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 97..106
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 166..175
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 195..216
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:2J66"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 279..291
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 294..300
FT /evidence="ECO:0007829|PDB:2J66"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 337..342
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 344..347
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 351..359
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 391..396
FT /evidence="ECO:0007829|PDB:2J66"
FT STRAND 399..404
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 409..413
FT /evidence="ECO:0007829|PDB:2J66"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:2J66"
SQ SEQUENCE 428 AA; 47816 MW; 4545F7F69D0AFEC7 CRC64;
MNLDQAEITA LTKRFETPFY LYDGDFIEAH YRQLRSRTNP AIQFYLSLKA NNNIHLAKLF
RQWGLGVEVA SAGELALARH AGFSAENIIF SGPGKKRSEL EIAVQSGIYC IIAESVEELF
YIEELAEKEN KTARVAIRIN PDKSFGSTAI KMGGVPRQFG MDESMLDAVM DAVRSLQFTK
FIGIHVYTGT QNLNTDSIIE SMKYTVDLGR NIYERYGIVC ECINLGGGFG VPYFSHEKAL
DIGKITRTVS DYVQEARDTR FPQTTFIIES GRYLLAQAAV YVTEVLYRKA SKGEVFVIVD
GGMHHHAAST FRGRSMRSNY PMEYIPVRED SGRRELEKVT IAGPLCTPED CLGKDVHVPA
LYPGDLVCVL NSGAYGLSFS PVHFLGHPTP IEILKRNGSY ELIRRKGTAD DIVATQLQTE
SNLLFVDK
